(data stored in ACNUC7421 zone)

SWISSPROT: C6B0F7_RHILS

ID   C6B0F7_RHILS            Unreviewed;       430 AA.
AC   C6B0F7;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
DE   RecName: Full=UDP-N-acetylglucosamine 1-carboxyvinyltransferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE            EC=2.5.1.7 {ECO:0000256|HAMAP-Rule:MF_00111};
DE   AltName: Full=Enoylpyruvate transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE   AltName: Full=UDP-N-acetylglucosamine enolpyruvyl transferase {ECO:0000256|HAMAP-Rule:MF_00111};
DE            Short=EPT {ECO:0000256|HAMAP-Rule:MF_00111};
GN   Name=murA {ECO:0000256|HAMAP-Rule:MF_00111};
GN   OrderedLocusNames=Rleg_0265 {ECO:0000313|EMBL:ACS54576.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54576.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54576.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54576.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
CC   -!- FUNCTION: Cell wall formation. Adds enolpyruvyl to UDP-N-
CC       acetylglucosamine. {ECO:0000256|HAMAP-Rule:MF_00111,
CC       ECO:0000256|SAAS:SAAS00767217}.
CC   -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + UDP-N-acetyl-alpha-D-
CC       glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-
CC       D-glucosamine. {ECO:0000256|HAMAP-Rule:MF_00111,
CC       ECO:0000256|SAAS:SAAS00767208}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767283}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
CC       ECO:0000256|SAAS:SAAS00767211}.
CC   -!- SIMILARITY: Belongs to the EPSP synthase family. MurA subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00111, ECO:0000256|SAAS:SAAS00767202}.
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DR   EMBL; CP001622; ACS54576.1; -; Genomic_DNA.
DR   RefSeq; WP_012755988.1; NC_012850.1.
DR   ProteinModelPortal; C6B0F7; -.
DR   EnsemblBacteria; ACS54576; ACS54576; Rleg_0265.
DR   KEGG; rlg:Rleg_0265; -.
DR   HOGENOM; HOG000075602; -.
DR   KO; K00790; -.
DR   OMA; CDPHRAT; -.
DR   OrthoDB; POG091H01PG; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008760; F:UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0019277; P:UDP-N-acetylgalactosamine biosynthetic process; IEA:InterPro.
DR   CDD; cd01555; UdpNAET; 1.
DR   Gene3D; 3.65.10.10; -; 2.
DR   HAMAP; MF_00111; MurA; 1.
DR   InterPro; IPR001986; Enolpyruvate_Tfrase_dom.
DR   InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b.
DR   InterPro; IPR005750; UDP_GlcNAc_COvinyl_MurA.
DR   Pfam; PF00275; EPSP_synthase; 1.
DR   SUPFAM; SSF55205; SSF55205; 1.
DR   TIGRFAMs; TIGR01072; murA; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6B0F7.
DR   SWISS-2DPAGE; C6B0F7.
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767221};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767191};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767246};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767261};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767234};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767219};
KW   Pyruvate {ECO:0000256|HAMAP-Rule:MF_00111};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00111,
KW   ECO:0000256|SAAS:SAAS00767179, ECO:0000313|EMBL:ACS54576.1}.
FT   DOMAIN        8    418       EPSP_synthase. {ECO:0000259|Pfam:
FT                                PF00275}.
FT   REGION       22     23       Phosphoenolpyruvate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   REGION      131    135       UDP-N-acetylglucosamine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   REGION      172    175       UDP-N-acetylglucosamine binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   ACT_SITE    126    126       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00111}.
FT   BINDING     102    102       UDP-N-acetylglucosamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   BINDING     317    317       UDP-N-acetylglucosamine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00111}.
FT   BINDING     339    339       UDP-N-acetylglucosamine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_00111}.
FT   MOD_RES     126    126       2-(S-cysteinyl)pyruvic acid O-
FT                                phosphothioketal. {ECO:0000256|HAMAP-
FT                                Rule:MF_00111}.
SQ   SEQUENCE   430 AA;  45744 MW;  5BA791E0B892AD41 CRC64;
     MDRIRIVGGN ELNGIIPISG AKNAALPLMI ASLLTSDTLT LENVPHLADV ELLMRILGNH
     GVDVAVNGRR ERQEDAYSRT IHFTCRTIVD TTASYELVSK MRASFWVIGP LLAREGHCRV
     SLPGGCAIGT RPVDLFIEGL TALGATMEID AGYINAKAPA GGLIGARYTF PKVSVGATHV
     MMMAATLARG TTVIGNAARE PEVVDLANCL NAMGARISGA GTATITIEGV TSLSGARHRV
     LPDRIETGTY AMAVAMAGGD VVLENTDVAL LETAVETLRR AGAEISSTNN GMRIKRNGAG
     IRPVDIVTDP FPGFPTDLQA QFMALMTRSS GVSHVTETIF ENRFMHVQEL ARLGARISLS
     GQTAKIEGVQ RLRGAPVMAT DLRASVSLVI AGLAAEGETT VSRVYHLDRG FERLEEKLTR
     CGAIVERISE
//

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